The Effect of Waste Fodder Potato Proteins on the Mechanical Properties of Carboxylated Acrylonitrile-Butadiene Rubber

Abstract

The current investigation treats about the influence of waste fodder potato proteins (WFPP) recovered from the starch industry on the mechanical-properties of carboxylated acrylonitrile-butadiene rubber (XNBR). WFPP were characterized and used as a filler of the above mentioned XNBR rubber without or after blending with zinc oxide. The obtained rubber compounds were cured, and mechanical properties such as tensile strength, hardness, and cross-linking density were investigated. It was found that the introduction of WFPP previously blended with zinc oxide into rubber compound increases the cross-linking density of the obtained composites, compared with the vulcanizate without protein, which in turn increases the mechanical properties of the obtained vulcanizates. That occurs thanks to the formation of ion nodes, as testified by equilibrium swelling. The introduction of WFPP into the elastomer matrix also increases the susceptibility of the elastomer to biodecomposition.

Commercial potato protein concentrate as a novel source for thermoformed bio-based plastic films with unusual polymerisation and tensile properties

“…So far, potato protein has formed a minor component in potato peel waste based materials (16 g protein per 100 g) 13 and has been used as a minor addition (5%) to carboxylated acrylonitrile-butadiene rubber. 27 In the former case, glycerol and lecithin were used to act as plasticizers and emulsiers, respectively, and high pressure homogenization was most effective in producing solutions for cast lms. In the latter case, potato proteins acted to increase the cross link density of vulcanizates and consequently improved mechanical properties, while simultaneously increasing biodegradability.…”

“…In the latter case, potato proteins acted to increase the cross link density of vulcanizates and consequently improved mechanical properties, while simultaneously increasing biodegradability. 27 Chemical and thermal denaturation during protein based material processing unfolds proteins exposing amino acid reactive groups. This unfolding makes reactive functional groups available for covalent bonding such as disulphide and isopeptide bonds, increases protein-protein interactions 28 and Maillard reactions with saccharides.…”